Exploration of Foods and Foodomics

Table 1

Interaction studies with various food additives, pesticides, and contaminants against different serum proteins.

Compound	Protein	Methods	Quenching mechanism	Quenching/Binding constant	Thermodynamic results	Binding region	Reference
Amaranth	HSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and molecular dynamics simulations (MDS)	Static	K_SV: 2.78 × 10⁴−3.76 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −11.8 kJ/mol ΔS° = 0.047 kJ‧mol^–1‧K^–1)	Subdomain IIA (site I)	[53]
New coccin	HSA		Static	K_SV: 4.1 × 10⁴−5.53 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −11.7 kJ/mol ΔS° = 0.050 kJ‧mol^–1‧K^–1 (Hydrogen bonding and electrostatic forces)	Subdomain IIA (site I)	[53]
Myricitrin	HSA	UV-Vis, fluorescence spectroscopy, CD, micro-FTIR, molecular docking, and MDS	Static	K_SV: 4.73 × 10⁴−5.76 × 10⁴ M^–1 K_a: 0.5 × 10⁵−3.48 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −16.23 kJ/mol ΔS° = 0.049 kJ‧mol^–1‧K^–1 (Hydrogen bonding, hydrophobic interactions, and electrostatic forces)	Subdomain IIA (site I)	[54]
Sodium tripolyphosphate	BSA	UV-Vis, fluorescence spectroscopy, FTIR, and molecular docking	Static	K_SV: 4.5 × 10³−9.38 × 10³ M^–1 K_a: 4.25 × 10¹ −2.23 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = −341.3 kJ/mol ΔS° = −1.064 kJ‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Subdomain IIA (Sudlow’s site I)	[55]
2,4,6-Trichlorophenol	BSA	UV-Vis, fluorescence spectroscopy, ITC, and molecular docking	Static	K_SV: 1.018 × 10⁶−1.692 × 10⁶ M^–1 K_a: 1.962 × 10⁵−5.701 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −58.06 kJ/mol ΔS° = −85.67 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Subdomain IIIA (site II)	[56]
2,4,6-Tribromophenol	BSA		Static	K_SV: 1.597 × 10⁶−2.941 × 10⁶ M^–1 K_a: 2.501 × 10⁵−15.385 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −98.97 kJ/mol ΔS° = −215.76 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Subdomain IIIA (site II)	[56]
Sodium hydrosulfite	BSA	UV-Vis, fluorescence spectroscopy, FTIR, molecular docking, and surface plasmon resonance (SPR)	Static and dynamic	K_SV: 5.13 × 10³−6.12 × 10³ M^–1 K_a: 0.313 × 10²−44.545 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −139,783 kJ/mol ΔS° = −404.592 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Subdomains IIA and IIIA (sites I and II)	[57]
Natamycin	BSA	UV-Vis, fluorescence spectroscopy, molecular docking, and SPR	Static and dynamic	K_SV: 5.32 × 10³−10.01 × 10³ M^–1 K_a: 2.13 × 10²−18.73 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −87.16 kJ/mol ΔS° = −237.6 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Subdomain IIIA (Sudlow’s site I)	[58]
Sunset yellow	HSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static	K_SV: 5.15 × 10⁴−6.8 × 10⁴ M^–1 K_a: 0.2 × 10⁶−3.11 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = −52.24 kJ/mol ΔS° = −50.07 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Sudlow’s site I	[59]
Allura red	HSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static	K_SV: 3.75 × 10⁴−4.21 × 10⁴ M^–1 K_a: 0.04 × 10⁶−0.3 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = −58.79 kJ/mol ΔS° = −115.1 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Sudlow’s site I	[59]
Propazine	BSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static	K_SV: 1.46 × 10³−1.60 × 10³ M^–1 K_a: 0.6 × 10^–3−9.55 × 10^–3 M^–1	ΔG° < 0 (spontaneous) ΔH° = −103.45 kJ/mol ΔS° = −0.05 kJ‧mol^–1‧K^–1 (Hydrogen bonding, hydrophobic interactions, and van der Waals forces)	Subdomains IIA and IIIA (sites I and II)	[60]
Quinoxyfen	BSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static	K_SV: 4.17 × 10³−6.39 × 10³ M^–1 K_a: 5.01 × 10²−7.08 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −12.84 kJ/mol ΔS° = 0.01 kJ‧mol^–1‧K^–1 (Hydrogen bonding, hydrophobic interactions, and van der Waals forces)	Subdomains IIA and IIIA (sites I and II)	[60]
Aclonifen	HSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Dynamic	K_SV: 1.62 × 10⁵−3.05 × 10⁵ M^–1 K_a: 0.0174 × 10⁶−1.95 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = 225.43 kJ/mol ΔS° = 0.864 kJ‧mol^–1‧K^–1 (Hydrophobic interactions)	Subdomains IIA and IIIA (sites I and II)	[61]
Bifenox	HSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Dynamic	K_SV: 1.6 × 10⁵−2.10 × 10⁵ M^–1 K_a: 0.002 × 10⁶−1.02 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = 304.63 kJ/mol ΔS° = 1.11 kJ‧mol^–1‧K^–1 (Hydrophobic interactions)	Subdomains IIA and IIIA (sites I and II)	[61]
Phosmet	Bovine hemoglobin (BHb)	UV-Vis, fluorescence spectroscopy, CD, FRET, and molecular docking	Dynamic	K_SV: 3.5 × 10^–6−4.8 × 10^–6 M^–1 K_a: 0.004 × 10³−6.4 × 10³ M^–1	ΔG° < 0 (spontaneous) ΔH° = −284.97 kJ/mol ΔS° = −88.29 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	NS	[62]
Isoflucypram	HSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, molecular docking, and MDS	Static and dynamic	K_SV: 1.593 × 10⁴–1.832 × 10⁴ M^–1 K_a: 0.158 × 10³−4.923 × 10³ M^–1	ΔG° < 0 (spontaneous) ΔH° = −187.549 kJ/mol ΔS° = −563.59 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Sudlow’s site I	[63]
Cuminaldehyde (4-isopropyl benzaldehyde)	HSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_SV: 5.5 × 10³–8.3 × 10³ M^–1	ΔG° < 0 (spontaneous) ΔH° = −16.0 kJ/mol ΔS° = 21.6 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)	Subdomain IIA (site I)	[64]
Cuminol (4-isopropyl benzyl alcohol)	HSA		Static	K_SV: 6.3 × 10²–9.4 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −15.9 kJ/mol ΔS° = 3.3 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)	Subdomain IIA (site I)	[64]
Potassium bromate	BSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static and dynamic	K_SV: 1.14 × 10⁴−1.36 × 10⁴ M^–1 K_a: 9.34 × 10³−2.93 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = −122.8 kJ/mol ΔS° = −320.51 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IB (site III)	[65]
Quinoline yellow	Lysozyme	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 94.55 × 10³−125.83 × 10³ M^–1 K_a: 5.69 × 10⁶−23.76 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = −49.02 kJ/mol ΔS° = −32.69 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	NS	[66]
Carbofuran	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_SV: 2.02 × 10⁴ M^–1 K_a: 1.17 × 10⁸ M^–1	NS	Site I	[67]
Naringenin	Lysozyme	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 24.28 × 10³−66.94 × 10³ M^–1 K_a: 53.74 × 10³−2,803.14 × 10³ M^–1	ΔG° < 0 (spontaneous) ΔH° = 259.13 kJ/mol ΔS° = 953.11 J‧mol^–1‧K^–1 (Hydrophobic interactions)	Trp 62, Trp 63, and Trp 108	[68]
Azinphos-methyl	BSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, and molecular docking	Dynamic	K_SV: 0.6 × 10⁴−1.46 × 10⁴ M^–1 K_a: 0.099 × 10⁵−0.209 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −133.25 kJ/mol ΔS° = −0.378 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IB (site III)	[69]
Flupyrimin	BSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, and molecular docking	Static	K_SV: 1.664 × 10⁴−1.921 × 10⁴ M^–1 K_a: 1.579 × 10⁵−1.907 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −14.36 kJ/mol ΔS° = 52.95 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)	Subdomain IIIA (site II)	[70]
Flupyrimin	HSA			K_SV: 1.909 × 10⁴−2.361 × 10⁴ M^–1 K_a: 1.706 × 10⁵−2.11 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −16.26 kJ/mol ΔS° = 47.31 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)
Nitenpyram	BSA			K_SV: 2.16 × 10⁴−2.349 × 10⁴ M^–1 K_a: 1.911 × 10⁵−2.108 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −7.51 kJ/mol ΔS° = 76.76 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)
Nitenpyram	HSA			K_SV: 2.225 × 10⁴−2.519 × 10⁴ M^–1 K_a: 1.994 × 10⁵−2.346 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −12.40 kJ/mol ΔS° = 61.16 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)
Formetanate hydrochloride	HSA	Fluorescence and CD spectroscopy, molecular docking, and MDS	Static	K_SV: 0.01−0.02 M^–1 K_a: 3.75 × 10^–5−5.14 × 10^–5 M^–1	ΔG° < 0 (spontaneous) ΔH° = 13.46 kJ/mol ΔS° = 0.15 J‧mol^–1‧K^–1 (Hydrophobic forces)	Sudlow’s site I and site II	[71]
Mancozeb	Hb	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 2.09 × 10⁴−3.27 × 10⁴ M^–1 K_a: 1.76 × 10⁴−5.33 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −10.35 kcal/mol ΔS° = −0.013 kcal‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	NS	[72]
Dicofol	HSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 0.73 × 10⁵−1.3 × 10⁵ M^–1 K_a: 0.82 × 10⁵−2.77 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −55.35 kJ/mol ΔS° = −84.7 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Suldow’s site I	[73]
Salicylic acid	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static and dynamic	K_SV: 10.26 M^–1	NS	Near the Trp-213	[74]
Beauvericin	HSA	UV-Vis, fluorescence spectroscopy, and molecular docking	NS	NS	NS	NS	[75]
Cyclopiazonic acid				logK_SV: 4.37 logK_a: 4.38		Sudlow’s site I
Sterigmatocystin				logK_SV: 4.32 logK_a: 3.98		NS
Butylated hydroxyanisole	BSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static	K_SV: 5.96 × 10³−9.3 × 10³ M^–1 K_a: 0.57 × 10⁴−3.18 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 110.8 kJ/mol ΔS° = 443.3 J‧mol^–1‧K^–1 (Hydrophobic forces)	Subdomain IIA (site I)	[76]
Sorbic acid	HSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, molecular docking, and MDS	Static	K_SV: 5.555 × 10⁴−6.218 × 10⁴ M^–1 K_a: 4.033 × 10⁵−5.046 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −29.366 kJ/mol ΔS° = 108.149 J‧mol^–1‧K^–1 (Hydrogen bonding, and hydrophobic forces)	Subdomain IIA (site I)	[77]
Dicyclohexyl phthalate	HSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, and molecular docking	Static	K_SV: 2.05 × 10⁵ M^–1 K_a: 13.47 × 10⁴−39.54 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −39.26 kJ/mol ΔS° = −29.14 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[78]
Monocyclohexyl phthalate	HSA		Static	K_SV: 1.24 × 10⁵ M^–1 K_a: 0.7 × 10⁴−1.72 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −43.18 kJ/mol ΔS° = −68.34 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[78]
Malachite green oxalate	HSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 374.9 M^–1 K_a: 4.35 × 10⁶ M^–1	ΔG° < 0 (spontaneous) (Hydrogen bonding, and van der Waals forces)	NS	[79]
Lutein dipalmitate	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Dynamic	K_SV: 2.17 × 10⁴−3.22 × 10⁴ M^–1 K_a: 0.63 × 10⁴−2.75 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −56.82 kJ/mol ΔS° = −106.02 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[80]
Chlorpyrifos	α₂M	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_SV: 1.017 × 10⁴−1.656 × 10⁴ M^–1 K_a: 5.432 × 10^–4−6.181 × 10^–4 M^–1	ΔG° < 0 (spontaneous) ΔH° = 15.62 kJ/mol ΔS° = 60.25 J‧mol^–1‧K^–1 (Hydrophobic forces)	Receptor-binding domain of the α₂M	[81]
Epoxiconazole	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_a: 0.79 × 10⁴−3.8 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −81.54 kJ/mol ΔS° = −199.35 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[82]
Epoxiconazole	HSA			K_a: 0.814 × 10⁴−6.22 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −105.74 kJ/mol ΔS° = −265.88 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)
Prothioconazole	BSA			K_a: 1.66 × 10⁵−6.45 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −84.85 kJ/mol ΔS° = −174.18 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)
Prothioconazole	HSA			K_a: 2.08 × 10⁵−5.75 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −64.39 kJ/mol ΔS° = −105.50 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)
Dicofol	HSA	UV-Vis, fluorescence spectroscopy, CD, ITC, and molecular docking	Static	K_SV: 1.18 × 10⁴−1.37 × 10⁴ M^–1 K_a: 4.38 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −5.42 kJ/mol ΔS° = 21.08 J‧mol^–1‧K^–1 (Hydrogen bonding, and hydrophobic forces)	Subdomain IIA (site I)	[83]
Thiamethoxam	Lysozyme	UV-Vis, fluorescence spectroscopy, molecular docking, and MDS	Static	K_SV: 0.2 × 10⁴−0.25 × 10⁴ M^–1 K_a: 0.12 × 10⁴−0.45 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 58.5 kJ/mol ΔS° = 372.55 J‧mol^–1‧K^–1 (Hydrophobic interactions)	NS	[84]
	BSA			K_SV: 1.1 × 10⁴−1.15 × 10⁴ M^–1 K_a: 1.93 × 10⁴−4.99 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 11.94 kJ/mol ΔS° = 231.88 J‧mol^–1‧K^–1 (Hydrophobic interactions)	Site I
	HSA			K_SV: 1.24 × 10⁴−1.35 × 10⁴ M^–1 K_a: 1.91 × 10⁴−2.41 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 12.84 kJ/mol ΔS° = 235.20 J‧mol^–1‧K^–1 (Hydrophobic interactions)	Site I
Phosmet	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_a: 0.15 × 10⁴−3.68 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −16.33 kJ/mol ΔS° = −469 kJ‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Sudlow’s site II	[85]
Phosmet	Lysozyme	UV-Vis, fluorescence spectroscopy, CD, FTIR, and molecular docking	Static	K_SV: 0.42 × 10⁴−1.51 × 10⁴ M^–1 K_a: 0.0168 × 10⁴−9.14 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −60.2 kJ/mol ΔS° = −187.78 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	NS	[86]
β-Resorcylic acid	Lysozyme	UV-Vis, fluorescence spectroscopy, CD, FRET, and molecular docking	Static	K_SV: 1.69 × 10³−5.15 × 10³ M^–1 K_a: 1.13 × 10³−4.68×10³ M^–1	ΔG° < 0 (spontaneous) ΔH° = −13.97 kcal/mol ΔS° = −29.42 cal‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Amino acid residues: Arg115, Arg119, Try124, and Gln123	[87]
Acenaphthene	BSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, and molecular docking	Static	K_SV: 1.98 × 10⁵ M^–1 K_a: 3.82 × 10⁵ M^–1	NS	Subdomain IB (site III)	[88]
Quinoline yellow	αLA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Dynamic	K_SV: 4.0 × 10^–4−4.4 × 10^–4 M^–1 K_a: 0.091 × 10^–5−0.955 × 10^–5 M^–1	ΔG° < 0 (spontaneous) ΔH° = 18.79 kcal/mol ΔS° = 83.71 cal‧mol^–1‧K^–1 (Hydrophobic interactions)	Central binding site of αLA	[89]
Monosodium glutamate	BSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static and dynamic	K_SV: 1.873 × 10³−2.836 × 10³ M^–1 K_a: 1.151 × 10¹ −4.05 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 243.903 kJ/mol ΔS° = 888.291 J‧mol^–1‧K^–1 (Hydrophobic interactions)	Sudlow’s site II	[90]
Calcium lactate	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static and dynamic	K_SV: 2.06 × 10³−3.21 × 10³ M^–1 K_a: 1.44 × 10²−2.9 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −7.493 kJ/mol ΔS° = 24.61 J‧mol^–1‧K^–1 (Electrostatic forces)	Sudlow’s site II (subdomain IIIA)	[91]
Sudan III	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_a: 5.83 × 10²−6.41 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −5.65 kJ/mol ΔS° = 53.8 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[92]
Rhodamine B	HSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, nuclear magnetic resonance (NMR), and molecular docking	Static	K_SV: 5.86 × 10⁴−6.23 × 10⁴ M^–1 K_a: 6.06 × 10⁴−6.35 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −2.99 kJ/mol ΔS° = 81.91 J‧mol^–1‧K^–1 (Electrostatic forces)	Subdomain IIA (site I)	[93]
Rosmarinic acid	HSA	UV-Vis, fluorescence spectroscopy, CD, ITC, molecular docking, and MDS	Static	K_SV: 1.5 × 10⁴−2.7 × 10⁴ M^–1 K_a: 0.36 × 10⁷−1.1 × 10⁷ M^–1	ΔG° < 0 (spontaneous) ΔH° = 11.7016 kcal/mol ΔS° = 71.1303 cal‧mol^–1‧K^–1 (Hydrophobic forces)	NS	[94]
5-Hydroxymethyl-2-furaldehyde	HSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_SV: 3.25 × 10⁴−4.91 × 10⁴ M^–1 K_a: 3.72 × 10⁴−5.25 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −30.02 kJ/mol ΔS° = −10.14 J/‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[95]
3,5,6-Trichloro-2-pyridinol	BSA	Fluorescence spectroscopy, NMR, and molecular docking	Static	K_SV: 2.1 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = 23.77 kJ/mol ΔS° = 146.98 J‧mol^–1‧K^–1 (Hydrophobic forces)	Subdomain IIA (site I)	[96]
Paraoxon methyl	BSA	Fluorescence spectroscopy, NMR, and molecular docking	Static	K_SV: 4.09 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 94.74 kJ/mol ΔS° = 372.93 J‧mol^–1‧K^–1 (Hydrophobic forces)	Subdomain IIA and IIIA (sites I and II)	[96]
Chlorpyrifos	HSA	Solid-phase microextraction (SPME), and molecular docking	NS	K_a: 1.42 × 10⁵ M^–1	NS	NS	[97]
Parathion-methyl				K_a: 1.45 × 10⁴−8.19 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −193.3 kJ/mol ΔS° = −543.7 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)
Malathion				K_a: 1.07 × 10⁴−4.02 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −147.7 kJ/mol ΔS° = −399.2 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIIA (site II)
Benthiavalicarb-isopropyl	HSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 4.41 × 10³−8.66 × 10³ M^–1 K_a: 0.032 × 10²−7.965 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −206.39 kJ/mol ΔS° = −654.93 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Hydrophobic cavity of HSA	[98]
Pendimethalin	HSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 7.17 × 10⁴−9.92 × 10⁴ M^–1 K_a: 8.47 × 10⁴−10.63 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −16.17 kJ/mol ΔS° = 45.78 J‧mol^–1‧K^–1 (Hydrophobic forces)	Subdomain IIA (Sudlow’s site I)	[99]
Tebuconazole	BSA	UV-Vis, fluorescence spectroscopy, and CD	Static	K_a: 2.25 × 10²−4.67 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −46.72 kJ/mol ΔS° = −105.67 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	NS	[100]
Perfluorooctanoic acid	HSA	UV-Vis, fluorescence spectroscopy, FTIR, and molecular docking	Static	K_SV: 1.076 × 10⁴−1.328 × 10⁴ M^–1 K_a: 0.4463 × 10⁴−0.6153 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −17.48 kJ/mol ΔS° = 13.53 J‧mol^–1‧K^–1 (Electrostatic forces)	Site I	[101]
Perfluorodecanoic acid	HSA		Static	K_SV: 1.431 × 10⁴−1.731 × 10⁴ M^–1 K_a: 1.4514 × 10⁴−2.6788 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −33.37 kJ/mol ΔS° = −27.91 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Site I	[101]
Acesulfame	HSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_SV: 0.81 × 10³−1.77 × 10³ M^–1 K_a: 1.74 × 10²−1.82 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −2.88 kJ/mol ΔS° = 33.66 J‧mol^–1‧K^–1 (Electrostatic forces)	Subdomain IIA (site I)	[102]

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K_sv is Stern-Volmer or quenching constant. K_a is binding constant. ΔG°: Gibbs free energy change; ΔH°: enthalpy change; ΔS°: entropy change. α₂M: alpha-2-macroglobulin; αLA: alpha-lactalbumin; NS: not stated